“…FAD allows studying the effect of dimer stacking, as dodecin traps FAD from solution in a closed conformation, forming a tryptophan-isoalloxazine-adenine-tryptophan instead of tryptophan-isoalloxazine-isoalloxazine-tryptophan aromatic tetrade (6). Steady-state and transient spectroscopy of FAD in solution demonstrated a quenching of the excited state of the flavin by interactions with the adenine subunit in the closed conformation (17,(45)(46)(47). If for the quenching mechanism the second aromatic moiety is important, one should notice a difference in the transient data for the different bound cofactors riboflavin and FAD, respectively.…”
Background: Dodecin prevents riboflavin from autodegradation and exerting photo-induced cellular stress. Results: Ultrafast depopulation of excited states and ground state recovery is observed by transient spectroscopy. Conclusion: Ultrafast electron transfer in combination with proton transfer is responsible for deactivation of flavin excited states. Significance: A comprehensive study of parameters in the binding pocket affecting the riboflavin quenching mechanism is given.
“…FAD allows studying the effect of dimer stacking, as dodecin traps FAD from solution in a closed conformation, forming a tryptophan-isoalloxazine-adenine-tryptophan instead of tryptophan-isoalloxazine-isoalloxazine-tryptophan aromatic tetrade (6). Steady-state and transient spectroscopy of FAD in solution demonstrated a quenching of the excited state of the flavin by interactions with the adenine subunit in the closed conformation (17,(45)(46)(47). If for the quenching mechanism the second aromatic moiety is important, one should notice a difference in the transient data for the different bound cofactors riboflavin and FAD, respectively.…”
Background: Dodecin prevents riboflavin from autodegradation and exerting photo-induced cellular stress. Results: Ultrafast depopulation of excited states and ground state recovery is observed by transient spectroscopy. Conclusion: Ultrafast electron transfer in combination with proton transfer is responsible for deactivation of flavin excited states. Significance: A comprehensive study of parameters in the binding pocket affecting the riboflavin quenching mechanism is given.
“…Since in this solvent the preferred conformational state of the molecule is a stacked one, the fluorescence is highly quenched by the adenine group, interacting via an electron transfer process, leading to a fast decay [1, 4,5]. The corresponding distribution of the time constant values obtained by the regularized fitting according to Eq.…”
Abstract. Fluorescence kinetics of flavin adenine dinucleotide was measured in a wide time and spectral range in different media, affecting its intra-end extramolecular interactions, and analyzed by a new method based on compressed sensing.
“…Ugyanakkor abszorpció kinetikai méréseket a molekula konformációjának változására vonatkozóan eddig még nem közöltek az irodalomban. [55,65].…”
Section: Koenzimekunclassified
“…Az irodalom alapján a szolvatációs válaszidő 800 fs körüli, amely a diffúz mozgást jellemzi vízben [162]. A ~800 fs-os élettartam és az alacsonyabb hullámhosszak felé eltolódott spektrum is a szolvatációs dinamikának tulajdonítható egy korábbi tanulmány alapján [55].…”
Section: A Fad Fluoreszcenciájának Mérése Különböző Mikrokörnyezetekbenunclassified
“…Az irodalomban általános az egyetértés, hogy a ns körüli életidővel rendelkező komponens a FAD nyitott, a pikoszekundumos időtartományba eső komponensek pedig az összehajtott konformációra jellemzőek, ahol a közelbe kerülő ADP csoport kioltja a flavin fluoreszcenciáját [55,56,163]. …”
Section: A Fad Fluoreszcenciájának Mérése Különböző Mikrokörnyezetekbenunclassified
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